Single domain antibodies for the knockdown of cytosolic and nuclear proteins.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractSingle domain antibodies (sdAbs) from camels or sharks comprise only the variable heavy chain domain. Human sdAbs comprise the variable domain of the heavy chain (VH) or light chain (VL) and can be selected from human antibodies. SdAbs are stable, nonaggregating molecules in vitro and in vivo compared to complete antibodies and scFv fragments. They are excellent novel inhibitors of cytosolic/nuclear proteins because they are correctly folded inside the cytosol in contrast to scFv fragments. SdAbs are unique because of their excellent specificity and possibility to target posttranslational modifications such as phosphorylation sites, conformers or interaction regions of proteins that cannot be targeted with genetic knockout techniques and are impossible to knockdown with RNAi. The number of inhibiting cytosolic/nuclear sdAbs is increasing and usage of synthetic single pot single domain antibody libraries will boost the generation of these fascinating molecules without the need of immunization. The most frequently selected antigenic epitopes belong to viral and oncogenic proteins, followed by toxins, proteins of the nervous system as well as plant- and drosophila proteins. It is now possible to select functional sdAbs against virtually every cytosolic/nuclear protein and desired epitope. The development of new endosomal escape protein domains and cell-penetrating peptides for efficient transfection broaden the application of inhibiting sdAbs. Last but not least, the generation of relatively new cell-specific nanoparticles such as polymersomes and polyplexes carrying cytosolic/nuclear sdAb-DNA or -protein will pave the way to apply cytosolic/nuclear sdAbs for inhibition of viral infection and cancer in the clinic.
AffiliationHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.
The following license files are associated with this item:
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-ShareAlike 3.0 United States
- Interference of HCV replication by cell penetrable human monoclonal scFv specific to NS5B polymerase.
- Authors: Thueng-in K, Thanongsaksrikul J, Jittavisutthikul S, Seesuay W, Chulanetra M, Sakolvaree Y, Srimanote P, Chaicumpa W
- Issue date: 2014
- Stability-Diversity Tradeoffs Impose Fundamental Constraints on Selection of Synthetic Human V<sub>H</sub>/V<sub>L</sub> Single-Domain Antibodies from <i>In Vitro</i> Display Libraries.
- Authors: Henry KA, Kim DY, Kandalaft H, Lowden MJ, Yang Q, Schrag JD, Hussack G, MacKenzie CR, Tanha J
- Issue date: 2017
- Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein.
- Authors: Liu JL, Shriver-Lake LC, Anderson GP, Zabetakis D, Goldman ER
- Issue date: 2017 Dec 12
- Single-domain antibodies and their utility.
- Authors: Baral TN, MacKenzie R, Arbabi Ghahroudi M
- Issue date: 2013 Nov 18
- Antigen recognition by single-domain antibodies: structural latitudes and constraints.
- Authors: Henry KA, MacKenzie CR
- Issue date: 2018 Aug/Sep